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    The BRCA1-interacting protein Obg-like ATPase 1 (OLA1) functions in centriole duplication. In this study, we show the role of the mitotic kinase Aurora A in the reduction of centrosomal OLA1. Aurora A binds to and polyubiquitinates OLA1, targeting it for proteasomal degradation. NIMA-related kinase 2 (NEK2) phosphorylates the T124 residue of OLA1, increases binding of OLA1 to Aurora A and OLA1 polyubiquitination by Aurora A, and reduces centrosomal OLA1 in G2 phase. The kinase activity of Aurora A suppresses OLA1 polyubiquitination. The decrease in centrosomal OLA1 caused by Aurora A-mediated polyubiquitination promotes the recruitment of pericentriolar material proteins in G2 phase. The E3 ligase activity of Aurora A is critical for centrosome amplification induced by its overexpression. The results suggest a dual function of Aurora A as an E3 ubiquitin ligase and a kinase in the regulation of centrosomal OLA1, which is essential for proper centrosome maturation in G2 phase. Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.

    Citation

    Zhenzhou Fang, Xingming Li, Yuki Yoshino, Moe Suzuki, Huicheng Qi, Hinari Murooka, Riko Katakai, Matsuyuki Shirota, Thi Anh Mai Pham, Ayako Matsuzawa, Kei Otsuka, Chikashi Ishioka, Takahiro Mori, Natsuko Chiba. Aurora A polyubiquitinates the BRCA1-interacting protein OLA1 to promote centrosome maturation. Cell reports. 2023 Aug 29;42(8):112850

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    PMID: 37481721

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